scholarly journals The action of acid proteinase from Aspergillus oryzae on soybean proteins.

1977 ◽  
Vol 41 (2) ◽  
pp. 409-410 ◽  
Author(s):  
Tadanobu NAKADAI ◽  
Seiichi NASUNO
Keyword(s):  
Aspergillus Oryzae ◽  
Acid Proteinase ◽  
Soybean Proteins

scholarly journals Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin

1975 ◽  
Vol 147 (1) ◽  
pp. 45-53 ◽  
Author(s):  
R Davidson ◽  
A Gertler ◽  
T Hofmann
Keyword(s):  
Aspergillus Oryzae ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Molecular Forms ◽  
Acid Proteinase ◽  
Sedimentation Analysis ◽  
Simple Tool ◽  
Purification And Properties ◽  
Yield And Purity

An acid proteinase from Aspergillus oryzae was isolated from a commercial powder by successive (NH4)2SO4 fractionation, acetone precipitation, and ion-exchange chromatography on phosphate- and DEAE-cellulose columns. The purified enzyme was found to be homogeneous by ultracentrifuge-sedimentation analysis (S20, W equal 3.63S), but electrofocusing in polyacrylamide gels and electrophoresis at pH 3.2 revealed that it consists of two very closely migrating bands. No difference in the amino acid composition and enzymic activities of the two partially separated bands could be detected, and it was concluded that the acid proteinase exists in two molecular forms. The enzyme activates bovine trypsinogen and chymotrypsinogen at pH 3.5 (the kappacat. and Km values at 35degrees C are 11.3S- minus 1, 0.10mM and 1.14S- minus 1, 0.18mM respectively). It hydrolyses the Phe-Phe bond of the synthetic pepsin substrates Z-His-Phe-Phe-OEt (kappacat. equal 1.65S- minus 1, Km equal 0.640mM at pH 3.5, 30degrees C) and Z-Ala-Ala-Phe-Phe-OPy4Pr (kappacat. equal 0.37S- minus 1, Km equal 0.037 mM at pH2.9, 39degrees C), where Z represents benzyloxycarbonyl and OPy4Pr represents 3-(4-pyridyl)-propyl 1-ester. Activation of bovine chymotrypsinogen results from the cleavage of the Arg(15)-Ile(16) bond in the zymogen. No other cleavages were observed. The use of A. oryzae proteinase provides a simple tool for the production of pi-chymotrypsin in good yield and purity.

Further evidence on differentiation of Aspergillus sojae from Aspergillus oryzae by electrophoretic patterns of cellulase, pectin-lyase, and acid proteinase

1974 ◽  
Vol 20 (3) ◽  
pp. 413-416 ◽  
Author(s):  
S. Nasuno
Keyword(s):  
Aspergillus Oryzae ◽  
Wheat Bran ◽  
Pectin Lyase ◽  
Acid Proteinase ◽  
Solid Culture ◽  
Aspergillus Sojae ◽  
Electrophoretic Patterns ◽  
Cultural Conditions ◽  
Electrophoretic Mobilities ◽  
Species Specific

Cellulase (β-1,4-glucan-4-glucanohydrolase, EC. 3.2.1.4), pectin-lyase (EC. 4.2.2.3), and acid proteinase (aspergillopeptidase A) (EC. 3.4.4.17) extracted from wheat bran solid culture of 23 strains of Aspergillus oryzae and 21 strains of Aspergillus sojae showed species-specific patterns on electrophoresis in polyacrylamide gels. The electrophoretic patterns of the cellulase were independent of age or cultural conditions. The pectin-lyase patterns were also independent of culture age except early phase of growth. The species-specific patterns were clear at the stage of the maximum production of acid proteinase. With the exception of one strain, no variation of the electrophoretic mobilities of these key enzymes were observed between the strains of the same species. The results provide further evidence to support the establishment of A. sojae as a species distinct from A. oryzae and the use of the electrophoretic zymograms as a taxonomic aid.

scholarly journals The Action of Peptidases from Aspergillus oryzae in Digestion of Soybean Proteins

1972 ◽  
Vol 36 (2) ◽  
pp. 261-268 ◽  
Author(s):  
Tadanobu NAKADAI ◽  
Seiichi NASUNO ◽  
Nobuyoshi IGUCHI
Keyword(s):  
Aspergillus Oryzae ◽  
Soybean Proteins

scholarly journals Engineering a recombination neutral protease I from Aspergillus oryzae to improve enzyme activity at acidic pH

RSC Advances ◽  
2020 ◽  
Vol 10 (51) ◽  
pp. 30692-30699
Author(s):  
Yucheng Hu ◽  
Tong Li ◽  
Zhui Tu ◽  
Qinghua He ◽  
Yanping Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Oryzae ◽  
Neutral Protease ◽  
Acidic Ph ◽  
Soybean Proteins ◽  
Neutral Proteases

Extracellular neutral proteases (NPs) in Aspergillus oryzae (A. oryzae) play a role in hydrolyzing soybean proteins into smaller peptides at pH about 7.5.

The Effects of Brinolase (Fibrinolytic Enzyme from Aspergillus Oryzae) on Platelet Aggregation of Dog and Man

1972 ◽  
Vol 28 (01) ◽  
pp. 031-048 ◽  
Author(s):  
W. H. E Roschlau ◽  
R Gage
Keyword(s):  
Platelet Aggregation ◽  
Aspergillus Oryzae ◽  
Degradation Products ◽  
Blood Platelet ◽  
Human Platelets ◽  
Fibrinolytic Enzyme ◽  
Inhibitory Effects ◽  
Blood Platelet Aggregation

SummaryInhibition of blood platelet aggregation by brinolase (fibrinolytic enzyme from Aspergillus oryzae) has been demonstrated with human platelets in vitro and with dog platelets in vivo and in vitro, using both ADP and collagen as aggregating stimuli. It is suggested that the optimal inhibitory effects of brinolase occur indirectly through the generation of plasma fibrinogen degradation products, without compromising platelet viability, rather than by direct proteolysis of platelet structures.

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